Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Novel inhibitor for prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis and details of substrate-recognition mechanism.

Journal of molecular biology - 18 Jan 2008

Xu Yue, Nakajima Yoshitaka, Ito Kiyoshi, Zheng Heng, Oyama Hiroshi, Heiser Ulrich, Hoffmann Torsten, Gärtner Ulf-Torsten, Demuth Hans-Ulrich, Yoshimoto Tadashi

Abstract excerpt

A new inhibitor, H-Ala-Ile-pyrrolidin-2-yl boronic acid, was developed as an inhibitor against prolyl tripeptidyl aminopeptidase with a K(i) value of 88.1 nM. The structure of the prolyl tripeptidyl aminopeptidase complexed with the inhibitor (enzyme-inhibitor complex) was determined at 2.2 A resolution. The inhibitor was bound to the active site through a covalent bond between Ser603 and the boron atom of the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Glutamic Acid
Share to Hydrogen Bonding

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Hydrolysis

Share to Hydrophobic and Hydrophilic Interactions

Share to Models, Chemical

Share to Porphyromonas gingivalis

Share to X-Ray Diffraction

Source

Identifiers

PMID: 18042490
DOI: 10.1016/j.jmb.2007.09.077

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Novel inhibitor for prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis and details of substrate-recognition mechanism.PMID 18042490Read ↗

Structural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity.Semantic proximity Read ↗

Kinetic and crystallographic analysis of mutant Escherichia coli aminopeptidase P: insights into substrate recognition and the mechanism of catalysis.Semantic proximity Read ↗

Mutagenesis for Improvement of Activity and Stability of Prolyl Aminopeptidase from Aspergillus oryzae.Semantic proximity Read ↗

Studies on the molecular docking and amino Acid residues involving in recognition of substrate in proline iminopeptidase by site-directed mutagenesis.Semantic proximity Read ↗

Mapping of the active site of glutamate carboxypeptidase II by site‐directed mutagenesisSemantic proximity Read ↗

Structural determinants of inhibition of Porphyromonas gingivalis gingipain K by KYT-36, a potent, selective, and bioavailable peptidase inhibitorSemantic proximity Read ↗

Asp- and Glu-specific Novel Dipeptidyl Peptidase 11 of Porphyromonas gingivalis Ensures Utilization of Proteinaceous Energy SourcesSemantic proximity Read ↗

Human prolidase and prolidase deficiency: an overview on the characterization of the enzyme involved in proline recycling and on the effects of its mutations.Semantic proximity Read ↗

Possible role of inter-domain salt bridges in oligopeptidase B from Trypanosoma brucei: critical role of Glu172 of non-catalytic β-propeller domain in catalytic activity and Glu490 of catalytic domain in stability of OPB.Semantic proximity Read ↗

Structural basis for broad specificity in alpha-lytic protease mutants.Semantic proximity Read ↗

Structure, function, and inhibition of a genomic/clinical variant of Porphyromonas gingivalis peptidylarginine deiminaseSemantic proximity Read ↗

Mutation in the substrate-binding site of aminopeptidase B confers new enzymatic properties.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.